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O76090 (BEST1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bestrophin-1
Alternative name(s):
TU15B
Vitelliform macular dystrophy protein 2
Gene names
Name:BEST1
Synonyms:VMD2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length585 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Forms calcium-sensitive chloride channels. Highly permeable to bicarbonate. Ref.3 Ref.7 Ref.8

Subunit structure

Tetramer or pentamers. May interact with PPP2CB and PPP2R1B By similarity.

Subcellular location

Cell membrane; Multi-pass membrane protein. Basolateral cell membrane Ref.9.

Tissue specificity

Predominantly expressed in the basolateral membrane of the retinal pigment epithelium.

Post-translational modification

Phosphorylated by PP2A By similarity.

Involvement in disease

Vitelliform macular dystrophy 2 (VMD2) [MIM:153700]: VMD2 is an autosomal dominant form of macular degeneration that usually begins in childhood or adolescence. VMD2 is characterized by typical 'egg-yolk' macular lesions due to abnormal accumulation of lipofuscin within and beneath the retinal pigment epithelium cells. Progression of the disease leads to destruction of the retinal pigment epithelium and vision loss.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.2 Ref.8 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.25 Ref.26

Retinitis pigmentosa 50 (RP50) [MIM:613194]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9

Adult-onset vitelliform macular dystrophy (AVMD) [MIM:608161]: A rare autosomal dominant disorder with incomplete penetrance and highly variable expression. Patients usually become symptomatic in the fourth or fifth decade of life with a protracted disease of decreased visual acuity.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.12

Bestrophinopathy, autosomal recessive (ARB) [MIM:611809]: A retinopathy characterized by loss of central vision, an absent electro-oculogram light rise, and electroretinogram anomalies.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9 Ref.24

Vitreoretinochoroidopathy, autosomal dominant (ADVIRC) [MIM:193220]: A disorder characterized by vitreoretinochoroidal dystrophy. The clinical presentation is variable. VRCP may be associated with cataract, nanophthalmos, microcornea, shallow anterior chamber, and glaucoma.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.23

Sequence similarities

Belongs to the bestrophin family.

Sequence caution

The sequence BAH12234.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAH13472.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processIon transport
Sensory transduction
Transport
Vision
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Retinitis pigmentosa
   DomainTransmembrane
Transmembrane helix
   LigandCalcium
Chloride
   Molecular functionChloride channel
Ion channel
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processchloride transmembrane transport

Inferred from direct assay PubMed 17003041. Source: GOC

chloride transport

Inferred from direct assay PubMed 17003041. Source: MGI

detection of light stimulus involved in visual perception

Inferred from electronic annotation. Source: Ensembl

ion transmembrane transport

Traceable author statement. Source: Reactome

regulation of calcium ion transport

Inferred from electronic annotation. Source: Ensembl

transepithelial chloride transport

Inferred from direct assay PubMed 17003041. Source: HGNC

transmembrane transport

Traceable author statement. Source: Reactome

visual perception

Traceable author statement Ref.2. Source: ProtInc

   Cellular_componentbasolateral plasma membrane

Inferred from direct assay PubMed 11050159Ref.9. Source: UniProtKB

chloride channel complex

Inferred from electronic annotation. Source: UniProtKB-KW

cytosol

Traceable author statement PubMed 17003041. Source: HGNC

integral component of membrane

Traceable author statement PubMed 10737974. Source: ProtInc

membrane

Traceable author statement PubMed 10737974. Source: ProtInc

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionchloride channel activity

Inferred from direct assay PubMed 17003041. Source: MGI

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O76090-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 3 (identifier: O76090-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-60: Missing.
     581-585: DEAHS → SVLHLNQGHC...EDFLGPGEGR
Isoform 4 (identifier: O76090-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-60: Missing.
     290-316: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 585585Bestrophin-1
PRO_0000143114

Regions

Topological domain1 – 2525Cytoplasmic Potential
Transmembrane26 – 4621Helical; Potential
Topological domain47 – 7024Extracellular Potential
Transmembrane71 – 9121Helical; Potential
Topological domain92 – 17887Cytoplasmic Potential
Transmembrane179 – 19921Helical; Potential
Topological domain200 – 22829Extracellular Potential
Intramembrane229 – 24921 Potential
Topological domain250 – 27021Extracellular Potential
Transmembrane271 – 29121Helical; Potential
Topological domain292 – 585294Cytoplasmic Potential

Natural variations

Alternative sequence1 – 6060Missing in isoform 3 and isoform 4.
VSP_008973
Alternative sequence290 – 31627Missing in isoform 4.
VSP_008975
Alternative sequence581 – 5855DEAHS → SVLHLNQGHCIALCPTPASL ALSLPFLHNFLGFHHCQSTL DLRPALAWGIYLATFTGILG KCSGPFLTSPWYHPEDFLGP GEGR in isoform 3.
VSP_008974
Natural variant31I → T in VMD2. Ref.26
VAR_058273
Natural variant61T → P in VMD2 and AVMD. Ref.2 Ref.26
Corresponds to variant rs28940275 [ dbSNP | Ensembl ].
VAR_000830
Natural variant61T → R in VMD2.
VAR_017366
Natural variant91V → A in VMD2.
VAR_000831
Natural variant91V → M in VMD2.
Corresponds to variant rs28940276 [ dbSNP | Ensembl ].
VAR_000832
Natural variant101A → T in VMD2.
VAR_000833
Natural variant101A → V in VMD2. Ref.11
VAR_010468
Natural variant111N → I in VMD2. Ref.20
VAR_017367
Natural variant131R → H in VMD2. Ref.10
VAR_010469
Natural variant161S → F in VMD2. Ref.16
VAR_010470
Natural variant171F → C in VMD2. Ref.16
VAR_010471
Natural variant211L → V in VMD2.
VAR_000834
Natural variant241W → C in VMD2.
VAR_000835
Natural variant251R → Q in VMD2.
VAR_000836
Natural variant251R → W in VMD2.
VAR_000837
Natural variant261G → R in VMD2. Ref.20
VAR_017368
Natural variant271S → R in VMD2.
VAR_000838
Natural variant291Y → H in VMD2. Ref.20
VAR_017369
Natural variant301K → R in VMD2.
VAR_017370
Natural variant411L → P in VMD2 and ARB. Ref.20 Ref.24
VAR_017371
Natural variant471R → H in AVMD.
Corresponds to variant rs28940278 [ dbSNP | Ensembl ].
VAR_017372
Natural variant581Q → L in VMD2.
VAR_000839
Natural variant671L → V.
VAR_000840
Natural variant731I → N in VMD2. Ref.16
VAR_010472
Natural variant801F → L in VMD2.
VAR_017373
Natural variant821L → V in VMD2. Ref.11 Ref.26
VAR_010473
Natural variant851Y → H in VMD2; loss of cloride and bicarbonate anions conduction. Ref.2 Ref.8
Corresponds to variant rs28940274 [ dbSNP | Ensembl ].
VAR_000841
Natural variant861V → M in ADVIRC. Ref.23
VAR_058274
Natural variant891V → A in VMD2. Ref.17
VAR_017374
Natural variant911T → I in VMD2.
VAR_017375
Natural variant921R → C in VMD2; loss of cloride and bicarbonate anions conduction. Ref.8 Ref.11
VAR_010474
Natural variant921R → H in VMD2. Ref.16
VAR_010475
Natural variant921R → S in VMD2.
VAR_000842
Natural variant931W → C in VMD2; loss of cloride and bicarbonate anions conduction. Ref.2 Ref.8 Ref.10
Corresponds to variant rs28940273 [ dbSNP | Ensembl ].
VAR_000843
Natural variant961Q → H in VMD2. Ref.11
VAR_010476
Natural variant991N → K in VMD2.
VAR_000844
Natural variant1001L → R in VMD2.
VAR_000845
Natural variant1011P → T in VMD2.
VAR_017376
Natural variant1021W → R in VMD2. Ref.20
VAR_017377
Natural variant1041D → E in VMD2.
VAR_000846
Natural variant1041D → H in VMD2. Ref.20
VAR_017378
Natural variant1051R → C in age-related macular degeneration. Ref.15
VAR_025731
Natural variant1131F → L in VMD2. Ref.22
VAR_025732
Natural variant1191E → Q in a sporadic case of concentric annular macular dystrophy.
Corresponds to variant rs1805142 [ dbSNP | Ensembl ].
VAR_010477
Natural variant1331N → K in VMD2.
VAR_017379
Natural variant1351G → S in VMD2. Ref.11
VAR_010478
Natural variant1401L → R in VMD2.
VAR_017380
Natural variant1401L → V in RP50; causes protein mislocalization to the cytoplasm and reduction of channel activity. Ref.9
VAR_063169
Natural variant1411R → H in VMD2 and ARB; reduced whole-cell conductance. Ref.24
Corresponds to variant rs121918284 [ dbSNP | Ensembl ].
VAR_000847
Natural variant1461A → K in AVMD; sporadic; requires 2 nucleotide substitutions. Ref.12
Corresponds to variant rs1800995 [ dbSNP | Ensembl ].
VAR_010479
Natural variant1521P → A in ARB; reduced whole-cell conductance. Ref.24
VAR_043493
Natural variant1951A → V in VMD2.
Corresponds to variant rs200277476 [ dbSNP | Ensembl ].
VAR_017381
Natural variant2011I → T in VMD2. Ref.15
VAR_025733
Natural variant2051I → T in RP50; reduced channel activity. Ref.9
VAR_063170
Natural variant2071L → I in VMD2. Ref.15
Corresponds to variant rs74653691 [ dbSNP | Ensembl ].
VAR_025734
Natural variant2091S → N in VMD2.
VAR_000848
Natural variant2161T → I in a sporadic case of age-related macular degeneration.
VAR_010480
Natural variant2181R → C in VMD2. Ref.10 Ref.11 Ref.16 Ref.25
VAR_000849
Natural variant2181R → H in VMD2. Ref.16
VAR_010481
Natural variant2181R → Q in VMD2.
VAR_000850
Natural variant2181R → S in VMD2. Ref.11
VAR_000851
Natural variant2211C → W in VMD2. Ref.13
VAR_025735
Natural variant2221G → V in a family affected by Leber congenital amaurosis/VMD2. Ref.14
VAR_025736
Natural variant2241L → M in VMD2.
VAR_000852
Natural variant2241L → P in VMD2. Ref.15
VAR_025737
Natural variant2271Y → C in RP50. Ref.9
VAR_000853
Natural variant2271Y → N in VMD2. Ref.2 Ref.26
Corresponds to variant rs28941469 [ dbSNP | Ensembl ].
VAR_000854
Natural variant2281D → N in RP50; causes protein mislocalization to the cytoplasm. Ref.9
VAR_063171
Natural variant2311S → R in VMD2.
VAR_000855
Natural variant2351V → L in VMD2. Ref.16
VAR_010482
Natural variant2351V → M in VMD2.
VAR_000856
Natural variant2361Y → C in ADVIRC. Ref.23
VAR_058275
Natural variant2371T → R in VMD2.
VAR_000857
Natural variant2391V → M in ADVIRC. Ref.23
VAR_058276
Natural variant2411T → N in VMD2. Ref.20
VAR_025738
Natural variant2421V → M in VMD2; late-onset of visual disturbance. Ref.25
VAR_058277
Natural variant2431A → T in VMD2. Ref.15
Corresponds to variant rs28940570 [ dbSNP | Ensembl ].
VAR_025739
Natural variant2431A → V in VMD2 and AVMD. Ref.26
Corresponds to variant rs28940570 [ dbSNP | Ensembl ].
VAR_000858
Natural variant2751V → I in age-related macular degeneration. Ref.15
VAR_025740
Natural variant2761F → L in VMD2. Ref.15
VAR_025741
Natural variant2931Q → K in VMD2. Ref.11
VAR_010483
Natural variant2941L → V in VMD2. Ref.20
VAR_025742
Natural variant2951I → T in VMD2. Ref.18
VAR_025743
Natural variant2951Missing in VMD2.
VAR_000859
Natural variant2961N → H in VMD2. Ref.15
VAR_025744
Natural variant2961N → S in VMD2. Ref.16
VAR_010484
Natural variant2971P → A in VMD2.
VAR_000860
Natural variant2971P → S in VMD2. Ref.12 Ref.21
Corresponds to variant rs1805143 [ dbSNP | Ensembl ].
VAR_010485
Natural variant2981F → S in VMD2. Ref.20
VAR_025745
Natural variant2991G → A in VMD2. Ref.26
VAR_058313
Natural variant2991G → E in VMD2. Ref.2
Corresponds to variant rs28941468 [ dbSNP | Ensembl ].
VAR_000861
Natural variant3001E → D in VMD2. Ref.10 Ref.12 Ref.21
Corresponds to variant rs1805144 [ dbSNP | Ensembl ].
VAR_010486
Natural variant3001E → K in VMD2.
VAR_000862
Natural variant3011D → E in VMD2. Ref.10
VAR_000863
Natural variant3011D → N in VMD2.
VAR_000864
Natural variant302 – 3043Missing in VMD2.
VAR_058278
Natural variant3021D → G in VMD2. Ref.15
VAR_025746
Natural variant3021D → H in VMD2. Ref.19
VAR_025747
Natural variant3021D → V in VMD2. Ref.15
VAR_025748
Natural variant3031D → E in VMD2. Ref.19
VAR_025749
Natural variant3051F → S in VMD2.
VAR_000865
Natural variant3061E → D in VMD2. Ref.15
VAR_025750
Natural variant3061E → G in VMD2. Ref.15
VAR_025751
Natural variant3071T → A in VMD2. Ref.15
VAR_025752
Natural variant3071T → I in VMD2. Ref.10
VAR_010487
Natural variant3081N → S in VMD2. Ref.19
VAR_025753
Natural variant3101I → T in VMD2.
VAR_000866
Natural variant3111V → G in VMD2.
VAR_000867
Natural variant3121D → N in AVMD and ARB; causes protein mislocalization to the cytoplasm. Ref.9 Ref.24
VAR_000868
Natural variant3171V → M in ARB. Ref.24
VAR_043494
Natural variant3251M → T in ARB. Ref.24
VAR_043495
Natural variant3571A → V. Ref.5
Corresponds to variant rs17854138 [ dbSNP | Ensembl ].
VAR_043496
Natural variant5251E → A. Ref.12
Corresponds to variant rs200582915 [ dbSNP | Ensembl ].
VAR_010488
Natural variant5571E → K. Ref.12
VAR_010489
Natural variant5611T → A. Ref.12
VAR_010490
Natural variant5671L → F in a sporadic case of age-related macular degeneration; unknown pathological significance.
Corresponds to variant rs148060787 [ dbSNP | Ensembl ].
VAR_010491
Natural variant5781E → V.
Corresponds to variant rs1800010 [ dbSNP | Ensembl ].
VAR_009278

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: D0629AAF65BA1ACD

FASTA58567,684
        10         20         30         40         50         60 
MTITYTSQVA NARLGSFSRL LLCWRGSIYK LLYGEFLIFL LCYYIIRFIY RLALTEEQQL 

        70         80         90        100        110        120 
MFEKLTLYCD SYIQLIPISF VLGFYVTLVV TRWWNQYENL PWPDRLMSLV SGFVEGKDEQ 

       130        140        150        160        170        180 
GRLLRRTLIR YANLGNVLIL RSVSTAVYKR FPSAQHLVQA GFMTPAEHKQ LEKLSLPHNM 

       190        200        210        220        230        240 
FWVPWVWFAN LSMKAWLGGR IRDPILLQSL LNEMNTLRTQ CGHLYAYDWI SIPLVYTQVV 

       250        260        270        280        290        300 
TVAVYSFFLT CLVGRQFLNP AKAYPGHELD LVVPVFTFLQ FFFYVGWLKV AEQLINPFGE 

       310        320        330        340        350        360 
DDDDFETNWI VDRNLQVSLL AVDEMHQDLP RMEPDMYWNK PEPQPPYTAA SAQFRRASFM 

       370        380        390        400        410        420 
GSTFNISLNK EEMEFQPNQE DEEDAHAGII GRFLGLQSHD HHPPRANSRT KLLWPKRESL 

       430        440        450        460        470        480 
LHEGLPKNHK AAKQNVRGQE DNKAWKLKAV DAFKSAPLYQ RPGYYSAPQT PLSPTPMFFP 

       490        500        510        520        530        540 
LEPSAPSKLH SVTGIDTKDK SLKTVSSGAK KSFELLSESD GALMEHPEVS QVRRKTVEFN 

       550        560        570        580 
LTDMPEIPEN HLKEPLEQSP TNIHTTLKDH MDPYWALENR DEAHS 

« Hide

Isoform 3 [UniParc].

Checksum: 4E105E710FC438BE
Show »

FASTA60469,096
Isoform 4 [UniParc].

Checksum: EB111B7121ADC566
Show »

FASTA49857,349

References

« Hide 'large scale' references
[1]"Mutations in a novel gene, VMD2, encoding a protein of unknown properties cause juvenile-onset vitelliform macular dystrophy (Best's disease)."
Marquardt A., Stoehr H., Passmore L.A., Kraemer F., Rivera A., Weber B.H.F.
Hum. Mol. Genet. 7:1517-1525(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VMD2.
[2]"Identification of the gene responsible for Best macular dystrophy."
Petrukhin K., Koisti M.J., Bakall B., Li W., Xie G., Marknell T., Sandgren O., Forsman K., Holmgren G., Andreasson S., Vujic M., Bergen A.A.B., McGarty-Dugan V., Figueroa D., Austin C.P., Metzker M.L., Caskey C.T., Wadelius C.
Nat. Genet. 19:241-247(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS VMD2 PRO-6; HIS-85; CYS-93; ASN-227 AND GLU-299.
[3]"Structure-function analysis of the bestrophin family of anion channels."
Tsunenari T., Sun H., Williams J., Cahill H., Smallwood P., Yau K.-W., Nathans J.
J. Biol. Chem. 278:41114-41125(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TOPOLOGY.
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), VARIANT VAL-357.
Tissue: Brain.
[6]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 52-585 (ISOFORM 1).
Tissue: Amygdala, Subthalamic nucleus and Synovium.
[7]"The vitelliform macular dystrophy protein defines a new family of chloride channels."
Sun H., Tsunenari T., Yau K.-W., Nathans J.
Proc. Natl. Acad. Sci. U.S.A. 99:4008-4013(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"Bestrophin Cl- channels are highly permeable to HCO3-."
Qu Z., Hartzell H.C.
Am. J. Physiol. 294:C1371-C1377(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CHARACTERIZATION OF VARIANTS VMD2 HIS-85; CYS-92 AND CYS-93.
[9]"Missense mutations in a retinal pigment epithelium protein, bestrophin-1, cause retinitis pigmentosa."
Davidson A.E., Millar I.D., Urquhart J.E., Burgess-Mullan R., Shweikh Y., Parry N., O'Sullivan J., Maher G.J., McKibbin M., Downes S.M., Lotery A.J., Jacobson S.G., Brown P.D., Black G.C., Manson F.D.
Am. J. Hum. Genet. 85:581-592(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, VARIANTS RP50 VAL-140; THR-205; CYS-227 AND ASN-228, CHARACTERIZATION OF VARIANTS RP50 VAL-140; THR-205 AND ASN-228, CHARACTERIZATION OF VARIANT ARB ASN-312.
[10]"Bestrophin gene mutations in patients with Best vitelliform macular dystrophy."
Caldwell G.M., Kakuk L.E., Griesinger I.B., Simpson S.A., Nowak N.J., Small K.W., Maumenee I.H., Rosenfeld P.J., Sieving P.A., Shows T.B., Ayyagari R.
Genomics 58:98-101(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS VMD2 HIS-13; CYS-93; CYS-218; ASP-300; GLU-301 AND ILE-307.
[11]"The mutation spectrum of the bestrophin protein -- functional implications."
Bakall B., Marknell T., Ingvast S., Koisti M.J., Sandgren O., Li W., Bergen A.A.B., Andreasson S., Rosenberg T., Petrukhin K., Wadelius C.
Hum. Genet. 104:383-389(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS VMD2 VAL-10; VAL-82; CYS-92; HIS-96; SER-135; CYS-218; SER-218 AND LYS-293.
[12]"Evaluation of the Best disease gene in patients with age-related macular degeneration and other maculopathies."
Allikmets R., Seddon J.M., Bernstein P.S., Hutchinson A., Atkinson A., Sharma S., Gerrard B., Li W., Metzker M.L., Wadelius C., Caskey C.T., Dean M., Petrukhin K.
Hum. Genet. 104:449-453(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS VMD2 SER-297 AND ASP-300, VARIANT AVMD LYS-146, VARIANTS GLN-119; ILE-216; ALA-525; LYS-557; ALA-561 AND PHE-567.
[13]"A novel spontaneous missense mutation in VMD2 gene is a cause of a Best macular dystrophy sporadic case."
Palomba G., Rozzo C., Angius A., Pierrottet C.O., Orzalesi N., Pirastu M.
Am. J. Ophthalmol. 129:260-262(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT VMD2 TRP-221.
[14]"Mutation analysis of 3 genes in patients with Leber congenital amaurosis."
Lotery A.J., Namperumalsamy P., Jacobson S.G., Weleber R.G., Fishman G.A., Musarella M.A., Hoyt C.S., Heon E., Levin A., Jan J., Lam B., Carr R.E., Franklin A., Radha S., Andorf J.L., Sheffield V.C., Stone E.M.
Arch. Ophthalmol. 118:538-543(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT VAL-222.
[15]"Allelic variation in the VMD2 gene in best disease and age-related macular degeneration."
Lotery A.J., Munier F.L., Fishman G.A., Weleber R.G., Jacobson S.G., Affatigato L.M., Nichols B.E., Schorderet D.F., Sheffield V.C., Stone E.M.
Invest. Ophthalmol. Vis. Sci. 41:1291-1296(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AGE-RELATED MACULAR DEGENERATION CYS-105 AND ILE-275, VARIANTS VMD2 THR-201; ILE-207; PRO-224; THR-243; LEU-276; HIS-296; GLY-302; VAL-302; ASP-306; GLY-306 AND ALA-307.
[16]"Identification of novel VMD2 gene mutations in patients with Best vitelliform macular dystrophy."
Marchant D., Gogat K., Boutboul S., Pequignot M., Sternberg C., Dureau P., Roche O., Uteza Y., Hache J.C., Puech B., Puech V., Dumur V., Mouillon M., Munier F.L., Schorderet D.F., Marsac C., Dufier J.-L., Abitbol M.
Hum. Mutat. 17:235-235(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS VMD2 PHE-16; CYS-17; ASN-73; HIS-92; CYS-218; HIS-218; LEU-235 AND SER-296.
[17]"Best's vitelliform macular dystrophy caused by a new mutation (Val89Ala) in the VMD2 gene."
Eksandh L., Bakall B., Bauer B., Wadelius C., Andreasson S.
Ophthalmic Genet. 22:107-115(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT VMD2 ALA-89.
[18]"Identification of a novel VMD2 mutation in Japanese patients with Best disease."
Yanagi Y., Sekine H., Mori M.
Ophthalmic Genet. 23:129-133(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT VMD2 THR-295.
[19]"Use of denaturing HPLC and automated sequencing to screen the VMD2 gene for mutations associated with Best's vitelliform macular dystrophy."
Marchant D., Gogat K., Dureau P., Sainton K., Sternberg C., Gadin S., Dollfus H., Brasseur G., Hache J.C., Dumur V., Puech V., Munier F.L., Schorderet D.F., Marsac C., Menasche M., Dufier J.-L., Abitbol M.
Ophthalmic Genet. 23:167-174(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS VMD2 HIS-302; GLU-303 AND SER-308.
[20]"Ten novel mutations in VMD2 associated with Best macular dystrophy (BMD)."
Kraemer F., Mohr N., Kellner U., Rudolph G., Weber B.H.F.
Hum. Mutat. 22:418-418(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS VMD2 ILE-11; ARG-26; HIS-29; PRO-41; ARG-102; HIS-104; ASN-241; VAL-294 AND SER-298.
[21]"Phenotype and genotype correlations in two best families."
Seddon J.M., Sharma S., Chong S., Hutchinson A., Allikmets R., Adelman R.A.
Ophthalmology 110:1724-1731(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS VMD2 SER-297 AND ASP-300.
[22]"Gene Symbol: VMD2. Disease: Best vitelliform macular dystrophy (VMD2)."
Li Y., Wang G.L., Dong B.
Hum. Genet. 114:608-608(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT VMD2 LEU-113.
[23]"Mutations of VMD2 splicing regulators cause nanophthalmos and autosomal dominant vitreoretinochoroidopathy (ADVIRC)."
Yardley J., Leroy B.P., Hart-Holden N., Lafaut B.A., Loeys B., Messiaen L.M., Perveen R., Reddy M.A., Bhattacharya S.S., Traboulsi E., Baralle D., De Laey J.-J., Puech B., Kestelyn P., Moore A.T., Manson F.D.C., Black G.C.M.
Invest. Ophthalmol. Vis. Sci. 45:3683-3689(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ADVIRC MET-86; CYS-236 AND MET-239.
[24]"Biallelic mutation of BEST1 causes a distinct retinopathy in humans."
Burgess R., Millar I.D., Leroy B.P., Urquhart J.E., Fearon I.M., De Baere E., Brown P.D., Robson A.G., Wright G.A., Kestelyn P., Holder G.E., Webster A.R., Manson F.D.C., Black G.C.M.
Am. J. Hum. Genet. 82:19-31(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ARB PRO-41; HIS-141; ALA-152; ASN-312; MET-317 AND THR-325, CHARACTERIZATION OF VARIANTS ARB HIS-141 AND ALA-152.
[25]"Mutation analysis of the VMD2 gene in Thai families with Best macular dystrophy."
Atchaneeyasakul L.O., Jinda W., Sakolsatayadorn N., Trinavarat A., Ruangvoravate N., Thanasombatskul N., Thongnoppakhun W., Limwongse C.
Ophthalmic Genet. 29:139-144(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS VMD2 CYS-218 AND MET-242.
[26]"Clinical and molecular genetic analysis of Best vitelliform macular dystrophy."
Boon C.J.F., Theelen T., Hoefsloot E.H., van Schooneveld M.J., Keunen J.E.E., Cremers F.P.M., Klevering B.J., Hoyng C.B.
Retina 29:835-847(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS VMD2 THR-3; PRO-6; VAL-82; ASN-227; VAL-243; ALA-299 AND 302-ASP--ASP-304 DEL.
+Additional computationally mapped references.

Web resources

VMD2 mutation database
Mutations of the VMD2 gene

Retina International's Scientific Newsletter

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF073500 expand/collapse EMBL AC list , AF073491, AF073492, AF073493, AF073494, AF073495, AF073496, AF073497, AF073498, AF073499 Genomic DNA. Translation: AAC64926.1.
AF057169 mRNA. Translation: AAC64343.1.
AF057170 mRNA. Translation: AAC64344.1.
AF073501 mRNA. Translation: AAC33766.1.
AY515704 mRNA. Translation: AAR99654.1.
CH471076 Genomic DNA. Translation: EAW73982.1.
CH471076 Genomic DNA. Translation: EAW73985.1.
BC015220 mRNA. Translation: AAH15220.1.
BC041664 mRNA. Translation: AAH41664.1.
AK289681 mRNA. Translation: BAF82370.1.
AK295998 mRNA. Translation: BAH12234.1. Different initiation.
AK301392 mRNA. Translation: BAH13472.1. Different initiation.
CCDSCCDS31580.1. [O76090-1]
CCDS44623.1. [O76090-3]
RefSeqNP_001132915.1. NM_001139443.1. [O76090-3]
NP_004174.1. NM_004183.3. [O76090-1]
XP_005274270.1. XM_005274213.1.
XP_005274272.1. XM_005274215.1.
UniGeneHs.524910.
Hs.712676.

3D structure databases

ProteinModelPortalO76090.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113279. 1 interaction.
MINTMINT-239943.
STRING9606.ENSP00000301774.

Protein family/group databases

TCDB1.A.46.1.1. the anion channel-forming bestrophin (bestrophin) family.

PTM databases

PhosphoSiteO76090.

Proteomic databases

PaxDbO76090.
PRIDEO76090.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000378042; ENSP00000367281; ENSG00000167995. [O76090-4]
ENST00000378043; ENSP00000367282; ENSG00000167995. [O76090-1]
ENST00000449131; ENSP00000399709; ENSG00000167995. [O76090-3]
ENST00000524926; ENSP00000432681; ENSG00000167995.
GeneID7439.
KEGGhsa:7439.
UCSCuc001nsr.2. human. [O76090-3]
uc001nss.3. human. [O76090-1]
uc001nst.3. human. [O76090-4]

Organism-specific databases

CTD7439.
GeneCardsGC11P061717.
GeneReviewsBEST1.
H-InvDBHIX0036211.
HGNCHGNC:12703. BEST1.
MIM153700. phenotype.
193220. phenotype.
607854. gene.
608161. phenotype.
611809. phenotype.
613194. phenotype.
neXtProtNX_O76090.
Orphanet99000. Adult-onset foveomacular vitelliform dystrophy.
3086. Autosomal dominant vitreoretinochoroidopathy.
139455. Autosomal recessive bestrophinopathy.
1243. Best vitelliform macular dystrophy.
263347. MRCS syndrome.
791. Retinitis pigmentosa.
PharmGKBPA162377454.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG315004.
HOVERGENHBG044928.
InParanoidO76090.
KOK13878.
OMARSGYHSA.
OrthoDBEOG7N0C43.
PhylomeDBO76090.
TreeFamTF315803.

Enzyme and pathway databases

ReactomeREACT_15518. Transmembrane transport of small molecules.

Gene expression databases

ArrayExpressO76090.
BgeeO76090.
CleanExHS_BEST1.
GenevestigatorO76090.

Family and domain databases

InterProIPR000615. Bestrophin.
IPR021134. Bestrophin/UPF0187.
[Graphical view]
PANTHERPTHR10736. PTHR10736. 1 hit.
PfamPF01062. Bestrophin. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSBEST1. human.
GeneWikiBestrophin_1.
GenomeRNAi7439.
NextBio29132.
PROO76090.
SOURCESearch...

Entry information

Entry nameBEST1_HUMAN
AccessionPrimary (citable) accession number: O76090
Secondary accession number(s): A8K0W6 expand/collapse secondary AC list , B7Z3J8, B7Z736, O75904, Q53YQ9, Q8IUR9, Q8IZ80
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1998
Last modified: July 9, 2014
This is version 142 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM